CONTRIBUTIONSMN formulated the present hypothesis and he was accountable for writing the report. NB produced essential revision for the manuscript. The original figures were produced by MN.
Li et al. Cellular Molecular Biology Letters (2016) 21:25 DOI 10.1186/s11658-016-0026-Cellular Molecular Biology LettersSHORT COMMUNICATIONOpen AccessThe identification of human aldo-keto reductase AKR7A2 as a novel cytoglobinbinding partnerXin Li, Shanshan Zou, Zhen Li, Gaotai Cai, Bohong Chen, Ping Wang and Wenqi Dong Correspondence: [email protected] Department of Biopharmaceutics, College of Laboratory Medicine and Biotechnology, Southern Medical University, 1838 North Guangzhou Avenue, Guangzhou 510515, ChinaAbstractCytoglobin (CYGB), a member on the globin household, is believed to protect cells from reactive oxygen and nitrogen species and take care of hypoxic circumstances and oxidative stress. Even so, its molecular mechanisms of action are certainly not clearly understood. By means of immunoprecipitation combined having a two-dimensional electrophoresis ass spectrometry assay, we identified a CYGB interactor: aldo-keto reductase loved ones 7 member A2 (AKR7A2). The interaction was further confirmed making use of yeast two-hybrid and co-immunoprecipitation assays. Our final results show that AKR7A2 physically interacts with CYGB.PLK1 Protein Species Key phrases: CYGB, AKR7A2, Protein-protein interactions, Yeast two-hybrid assay, Co-immunoprecipitation, 2-DE, Oxidative stressIntroduction Cytoglobin (CYGB), which is a member with the globin loved ones, was found greater than a decade ago inside a proteomic screen of fibrotic liver [1].INPP5A Protein web It was originally named STAP (stellate activating protein). Human CYGB is a 190-amino acid, 21-kDa protein [2], encoded by a single copy gene mapped at the 17q25.PMID:24025603 three chromosomal segment [3]. It includes a compact helical conformation, giving it the capacity to bind to heme, which permits reversible binding of gaseous, diatomic molecules, including oxygen (O2), nitric oxide (NO) and carbon monoxide (CO), just like hemoglobin (Hb), myoglobin (Mb) and neuroglobin (Ngb) [4]. As opposed to those loved ones members, that are respectively localized inside the erythrocytes, muscles and neurons and neuroendocrine tissue, CYGB is expressed across a broad spectrum of vertebrate organs and tissues with varying expression levels. It’s identified predominantly within the fibroblasts of connective tissue and in fibroblast-related cell lineages, for instance chondroblasts, osteoblasts, hepatic stellate cells (HSCs) and myofibroblasts, and it may play a function in fibrotic organ disorder [3, 5]. Offered its similarity to other globins (especially Mb and Ngb), a number of respiratory and stress-related activities for CYGB have already been regarded as. These include things like oxygen storage, transport and sensing, terminal oxidase activity, nitric oxide dioxygenase activity [6], and scavenging of reactive oxygen species (ROS) [7]. It can be also believed to shield cells from reactive oxygen and nitrogen species and take care of hypoxic conditions and oxidative strain inside the cells [8]. CYGB is associated with numerous ailments,The Author(s). 2016 Open Access This article is distributed beneath the terms from the Inventive Commons Attribution 4.0 International License (://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, offered you give proper credit to the original author(s) and the source, offer a link to the Inventive Commons license, and indicate if modifications were made. The Creative Commons Public Domain De.
